Characterization of N-glycosylated type I collagen in streptozotocin-induced diabetes.
The N epsilon-glycosylation of lysine and hydroxylysine residues in collagen from streptozotocin-induced-diabetic rats was confirmed and the stability of the complex shown to be due to an Amadori rearrangement. The studies also demonstrate the relative specificities of glucose, galactose and mannose in their reaction with collagen. The glycosylation of lysine in vitro occurs with glucose and galactose, but not with mannose, whereas only gucose reacts with hydroxylysine to any significant extent. Glycosylation of collagen occurs slowly during normal aging, but in contrast with reports suggesting accelerated aging of collagen in diabetic animals, we clearly demonstrated that the apparent increased stability is not due to an acceleration of the normal maturation process involving the reducible cross-links.
D000818:Animals; D001894:Borohydrides; D055598:Chemical Phenomena; D002621:Chemistry; D003094:Collagen / Q000031:analogs & derivatives* / Q000378:metabolism; D003921:Diabetes Mellitus, Experimental / Q000378:metabolism*; D006027:Glycosides / Q000378:metabolism; D006601:Hexoses / Q000378:metabolism; D006901:Hydroxylysine / Q000378:metabolism; D066298:In Vitro Techniques; D008239:Lysine / Q000378:metabolism; D008297:Male; D010084:Oxidation-Reduction; D051381:Rats; D011919:Rats, Inbred Strains; D013710:Tendons / Q000378:metabolism
D001894:Borohydrides; D006027:Glycosides; D006601:Hexoses; C022814:glycosylated collagen; D006901:Hydroxylysine; D003094:Collagen; D008239:Lysine